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Sem1 links proteasome stability and specificity to multicellular development
The transition from vegetative growth to multicellular development represents an evolutionary hallmark linked to an oxidative stress signal and controlled protein degradation. We identified the Sem1 proteasome subunit, which connects stress response and cellular differentiation. The sem1 gene encode...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5821377/ https://www.ncbi.nlm.nih.gov/pubmed/29401458 http://dx.doi.org/10.1371/journal.pgen.1007141 |
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author | Kolog Gulko, Miriam Heinrich, Gabriele Gross, Carina Popova, Blagovesta Valerius, Oliver Neumann, Piotr Ficner, Ralf Braus, Gerhard H. |
author_facet | Kolog Gulko, Miriam Heinrich, Gabriele Gross, Carina Popova, Blagovesta Valerius, Oliver Neumann, Piotr Ficner, Ralf Braus, Gerhard H. |
author_sort | Kolog Gulko, Miriam |
collection | PubMed |
description | The transition from vegetative growth to multicellular development represents an evolutionary hallmark linked to an oxidative stress signal and controlled protein degradation. We identified the Sem1 proteasome subunit, which connects stress response and cellular differentiation. The sem1 gene encodes the fungal counterpart of the human Sem1 proteasome lid subunit and is essential for fungal cell differentiation and development. A sem1 deletion strain of the filamentous fungus Aspergillus nidulans is able to grow vegetatively and expresses an elevated degree of 20S proteasomes with multiplied ATP-independent catalytic activity compared to wildtype. Oxidative stress induces increased transcription of the genes sem1 and rpn11 for the proteasomal deubiquitinating enzyme. Sem1 is required for stabilization of the Rpn11 deubiquitinating enzyme, incorporation of the ubiquitin receptor Rpn10 into the 19S regulatory particle and efficient 26S proteasome assembly. Sem1 maintains high cellular NADH levels, controls mitochondria integrity during stress and developmental transition. |
format | Online Article Text |
id | pubmed-5821377 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-58213772018-03-15 Sem1 links proteasome stability and specificity to multicellular development Kolog Gulko, Miriam Heinrich, Gabriele Gross, Carina Popova, Blagovesta Valerius, Oliver Neumann, Piotr Ficner, Ralf Braus, Gerhard H. PLoS Genet Research Article The transition from vegetative growth to multicellular development represents an evolutionary hallmark linked to an oxidative stress signal and controlled protein degradation. We identified the Sem1 proteasome subunit, which connects stress response and cellular differentiation. The sem1 gene encodes the fungal counterpart of the human Sem1 proteasome lid subunit and is essential for fungal cell differentiation and development. A sem1 deletion strain of the filamentous fungus Aspergillus nidulans is able to grow vegetatively and expresses an elevated degree of 20S proteasomes with multiplied ATP-independent catalytic activity compared to wildtype. Oxidative stress induces increased transcription of the genes sem1 and rpn11 for the proteasomal deubiquitinating enzyme. Sem1 is required for stabilization of the Rpn11 deubiquitinating enzyme, incorporation of the ubiquitin receptor Rpn10 into the 19S regulatory particle and efficient 26S proteasome assembly. Sem1 maintains high cellular NADH levels, controls mitochondria integrity during stress and developmental transition. Public Library of Science 2018-02-05 /pmc/articles/PMC5821377/ /pubmed/29401458 http://dx.doi.org/10.1371/journal.pgen.1007141 Text en © 2018 Kolog Gulko et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Kolog Gulko, Miriam Heinrich, Gabriele Gross, Carina Popova, Blagovesta Valerius, Oliver Neumann, Piotr Ficner, Ralf Braus, Gerhard H. Sem1 links proteasome stability and specificity to multicellular development |
title | Sem1 links proteasome stability and specificity to multicellular development |
title_full | Sem1 links proteasome stability and specificity to multicellular development |
title_fullStr | Sem1 links proteasome stability and specificity to multicellular development |
title_full_unstemmed | Sem1 links proteasome stability and specificity to multicellular development |
title_short | Sem1 links proteasome stability and specificity to multicellular development |
title_sort | sem1 links proteasome stability and specificity to multicellular development |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5821377/ https://www.ncbi.nlm.nih.gov/pubmed/29401458 http://dx.doi.org/10.1371/journal.pgen.1007141 |
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